ISGylation和E3泛素酶:大西洋鱼的遗传视角
Unni Grimholt1, Hilde Sindre1, Arvind Y M Sundaram1,2
1Fish Health Research Section, Norwegian Veterinary Institute, Ås, Norway.
Frontiers in immunology
|July 9, 2025
概括
大西洋鱼心细胞被用来研究无素-蛋白酶体通路及其在抗病毒防御中对传染性鱼贫血病毒 (ISAV) 的作用. ISG15基因和特定的HERC基因被上调,表明它们参与了抗病毒反应.
科学领域:
- * 分子生物学 * 分子生物学
- * 免疫学 免疫学
- * 鱼类病毒学 鱼类病毒学
背景情况:
- * 无素-蛋白酶体通路对于哺乳动物宿主抗病毒反应至关重要,向病毒基因进行降解.
- *ISG15 (干扰素刺激基因15) 是一种类似于乌比奎丁的蛋白质修饰剂,通过ISGylation在抗病毒防御中起着重要作用.
- *在大西洋鱼中,心脏内皮细胞是传染性鱼贫血病毒 (ISAV) 的首要目标.
研究的目的:
- *建立和描述来自大西洋鱼心脏组织 (ASH2-2) 的新细胞系,作为研究ISAV感染的模型.
- * 调查ISAV感染和重组干扰素 (rIFNg) 对大西洋鱼内皮细胞中涉及至基因素-蛋白酶体通路的基因的影响.
- * 确定与ISGylation相关的特异性基因及其在抗病毒防御中的潜在作用.
主要方法:
- *从大西洋鱼心脏组织中建立ASH2-2细胞系.
- *ASH2-2细胞感染ISAV,并使用rIFNg进行治疗.
- *使用转录组学进行基因表达分析,以评估抗病毒和无素-蛋白酶体通路基因的上调调节.
- *植物遗传学分析,以确定特异的HERC基因集群.
主要成果:
- *ASH2-2细胞系表现出内皮状特征,对ISAV感染具有宽容性,通过病毒传感器的上调反应.
- * 两种ISG15基因在感染后48小时 (p.i.) 显著上调. 作为对ISAV的回应.
- * 遗传学分析揭示了特异的HERC8和HERC9基因集群. 大西洋鱼的复制基因HERC7和HERC9在每天24小时被ISAV和rIFNg上调,而HERC8基因受到的影响较小.
- * 一个USP18复制品早在下午4点就显示出强烈的上调,这表明ISGylation过程的早期调节.
结论:
- * 该研究成功地建立并利用了一种新的大西洋鱼心脏内皮细胞系 (ASH2-2) 用于ISAV感染研究.
- *结果表明ISG15,HERC7,HERC9和USP18基因可能参与大西洋鱼对ISAV的抗病毒反应.
- *需要进行进一步的功能研究,以阐明这些候选基因在乌比奎丁-蛋白酶体通路和远程体中抗病毒防御中的精确作用.
相关概念视频
Oligosaccharide Assembly
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
Protein Modifications in the RER
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.


